| http://purl.uniprot.org/citations/24043427 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24043427 | http://www.w3.org/2000/01/rdf-schema#comment | "Ethylene is an important plant hormone that regulates numerous cellular processes and stress responses. The mode of action of ethylene is both dose- and time-dependent. Protein phosphorylation plays a key role in ethylene signaling, which is mediated by the activities of ethylene receptors, constitutive triple response 1 (CTR1) kinase, and phosphatase. To address how ethylene alters the cellular protein phosphorylation profile in a time-dependent manner, differential and quantitative phosphoproteomics based on (15)N stable isotope labeling in Arabidopsis was performed on both one-minute ethylene-treated Arabidopsis ethylene-overly-sensitive loss-of-function mutant rcn1-1, deficient in PP2A phosphatase activity, and a pair of long-term ethylene-treated wild-type and loss-of-function ethylene signaling ctr1-1 mutants, deficient in mitogen-activated kinase kinase kinase activity. In total, 1079 phosphopeptides were identified, among which 44 were novel. Several one-minute ethylene-regulated phosphoproteins were found from the rcn1-1. Bioinformatic analysis of the rcn1-1 phosphoproteome predicted nine phosphoproteins as the putative substrates for PP2A phosphatase. In addition, from CTR1 kinase-enhanced phosphosites, we also found putative CTR1 kinase substrates including plastid transcriptionally active protein and calcium-sensing receptor. These regulatory proteins are phosphorylated in the presence of ethylene. Analysis of ethylene-regulated phosphosites using the group-based prediction system with a protein-protein interaction filter revealed a total of 14 kinase-substrate relationships that may function in both CTR1 kinase- and PP2A phosphatase-mediated phosphor-relay pathways. Finally, several ethylene-regulated post-translational modification network models have been built using molecular systems biology tools. It is proposed that ethylene regulates the phosphorylation of arginine/serine-rich splicing factor 41, plasma membrane intrinsic protein 2A, light harvesting chlorophyll A/B binding protein 1.1, and flowering bHLH 3 proteins in a dual-and-opposing fashion."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.org/dc/terms/identifier | "doi:10.1074/mcp.m113.031633"xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Cheng H."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Hu Q."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Li J."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Li N."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Liu C.Y."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Xue Y."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Yang Z."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Zhang M."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Guo G."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/author | "Lam H."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/name | "Mol Cell Proteomics"xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/pages | "3559-3582"xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/title | "Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase."xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/24043427 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24043427 |
| http://purl.uniprot.org/citations/24043427 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24043427 |
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| http://purl.uniprot.org/uniprot/#_A0A178WIF0-mappedCitation-24043427 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24043427 |
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| http://purl.uniprot.org/uniprot/#_Q05609-mappedCitation-24043427 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24043427 |
| http://purl.uniprot.org/uniprot/#_P43286-mappedCitation-24043427 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24043427 |